Crystallin protein (misfolded form)

Misfolded lens proteins—primarily crystallins such as α-, β-, and γ-crystallin—are structural proteins in the lens that, when destabilized by mutations or post-translational modifications (oxidation, truncation, deamidation), lose their normal soluble, transparent state and aggregate to form light-scattering opacities characteristic of cataract[1][3][6]. α-crystallin also functions as a molecular chaperone, sequestering misfolded proteins; when overwhelmed or mutated, aggregation is accelerated, leading to further lens opacification and sometimes cell death[1][2][5]. The process is central to cataract pathogenesis, but "misfolded lens proteins" describes a phenotype rather than a discrete, druggable molecular entity or validated therapeutic target[3]. Thus, it is not a canonical target but rather a pathogenic state or consequence of damaged crystallin homeostasis.

Other names

Misfolded lens crystallinsAggregated crystallinMisfolded α-crystallinMisfolded β-crystallinMisfolded γ-crystallin

None standard; experimental strategies aim to prevent aggregation, stabilize folding, or enhance clearance